IndraLab

Statements


USP44 deubiquitinates FOXP3. 8 / 8
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"Notably, TGF-β-induced USP44 exhibits an obvious synergistic effect with USP7, and the coexpression of USP44 and USP7 almost completely eliminates Foxp3 polyubiquitination [164]."

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"Similarly, USP21, USP22, and USP44 also deubiquitinate Foxp3, preventing its degradation (195–199)."

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"It is reported that the differentiation of Tregs is promoted by USP44 through facilitating the deubiquitination of FOXP3 (Yang et al., 2020a)."

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"USP44 cooperates with USP7 to mediate the deubiquitination and stabilization of Foxp3, thus modulating Treg function (31)."

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"Interestingly, USP44 co-operated with USP7 to deubiquitinate and stabilize FOXP3."

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"To this end, we characterized the deubiquitination of FOXP3 by USP44 invitro in the presence of wild-type ubiquitin molecules and mutants lacking all but specific lysine residues."

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"USP44 co-operates with USP7 to deubiquitinate FOXP3 and stabilize expression."

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"We therefore investigated whether or not USP44 co-operates with USP7 to deubiquitinate and preserve FOXP3."